참고문헌
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- Davis, J., T. J. Donohue, and S. Kaplan. 1988. Construction, characterization, and complementation of a Puf- mutant of Rhodobacter sphaeroides. J. Bacteriol. 170, 320-329 https://doi.org/10.1128/jb.170.1.320-329.1988
- Dryden, S. C., and S. Kaplan. 1990. Localization and structural analysis of the ribosomal RNA operons of Rhodobacter sphaeroides. Nucleic Acids Res. 18, 7267-7277 https://doi.org/10.1093/nar/18.24.7267
- Elsen, S., W. Dischert, A. Colbeau, and C. E. Bauer. 2000. Expression of uptake hydrogenase and molybdenum nitrogenase in Rhodobacter capsulatus is coregulated by the RegB-RegA two-component regulatory system. J. Bacteriol. 182, 2831-2837 https://doi.org/10.1128/JB.182.10.2831-2837.2000
- Eraso, J. M., and S. Kaplan. 1994. prrA, a putative response regulator involved in oxygen regulation of photosynthesis gene expression in Rhodobacter sphaeroides. J. Bacteriol. 176, 32-43 https://doi.org/10.1128/jb.176.1.32-43.1994
- Eraso, J. M., and S. Kaplan. 1995. Oxygen-insensitive synthesis of the photosynthetic membranes of Rhodobacter sphaeroides: a mutant histidine kinase. J. Bacteriol. 177, 2695-2706 https://doi.org/10.1128/jb.177.10.2695-2706.1995
- Eraso, J. M., and S. Kaplan. 1996. Complex regulatory activities associated with the histidine kinase PrrB in expression of photosynthesis genes in Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 178, 7037-7046 https://doi.org/10.1128/jb.178.24.7037-7046.1996
- Gomelsky, M., I. M. Horne, H. J. Lee, J. M. Pemberton, A.G. McEwan, and S. Kaplan. 2000. Domain structure, oligomeric state, and mutational analysis of PpsR, the Rhodobacter sphaeroides repressor of photosystem gene expression. J. Bacteriol. 182, 2253-2261 https://doi.org/10.1128/JB.182.8.2253-2261.2000
- Gomelsky, M., and S. Kaplan. 1995. appA, a novel gene encoding a trans-acting factor involved in the regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 177, 4609-4618 https://doi.org/10.1128/jb.177.16.4609-4618.1995
- Gomelsky, M., and S. Kaplan. 1995. Genetic evidence that PpsR from Rhodobacter sphaeroides 2.4.1 functions as a repressor of puc and bchF expression. J. Bacteriol. 177, 1634-1637 https://doi.org/10.1128/jb.177.6.1634-1637.1995
- Gomelsky, M., and S. Kaplan. 1997. Molecular genetic analysis suggesting interactions between AppA and PpsR in regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 179, 128-134 https://doi.org/10.1128/jb.179.1.128-134.1997
- Gomelsky, M., and S. Kaplan. 1998. AppA, a redox regulator of photosystem formation in Rhodobacter sphaeroides 2.4.1, is a flavoprotein. Identification of a novel FAD binding domain. J. Biol. Chem. 273, 35319-35325 https://doi.org/10.1074/jbc.273.52.35319
- Happ, H. N., S. Braatsch, V. Broschek, L. Osterloh, and G. Klug. 2005. Light-dependent regulation of photosynthesis genes in Rhodobacter sphaeroides 2.4.1 is coordinately controlled by photosynthetic electron transport via the PrrBA two-component system and the photoreceptor AppA. Mol. Microbiol. 58, 903-914 https://doi.org/10.1111/j.1365-2958.2005.04882.x
- Horne, I. M., J. M. Pemberton, and A. McEwan. 1996. Photosynthesis gene expression in Rhodobacter sphaeroides is regulated by redox changes which are linked to electron transport. Microbiology 142, 2831-2838 https://doi.org/10.1099/13500872-142-10-2831
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- Yeliseev, A. A., J. M. Eraso, and S. Kaplan. 1996. Differential carotenoid composition of the B875 and B800-850 photosynthetic antenna complexes in Rhodobacter sphaeroides 2.4.1: involvement of spheroidene and spheroidenone in adaptation to changes in light intensity and oxygen availability. J. Bacteriol. 178, 5877-5883
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- Zeilstra-Ryalls, J. H., K. Gabbert, N. J. Mouncey, S. Kaplan, and R. G. Kranz. 1997. Analysis of the fnrL gene and its function in Rhodobacter capsulatus. J. Bacteriol. 179, 7264-7273 https://doi.org/10.1128/jb.179.23.7264-7273.1997
- Zeilstra-Ryalls, J. H., and S. Kaplan. 1998. Role of the fnrL gene in photosystem gene expression and photosynthetic growth of Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 180, 1496-1503